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Title: Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode

Abstract

We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k° ET, of 0.4 s -1 for the native form and 0.55 s -1 for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k° ET = 8.0·10 -3 cm·s -1 at pH 7.07. In conclusion, modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications formore » describing chemical transformations at biological-mineral interfaces.« less

Authors:
ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [1]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1530101
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Bioelectrochemistry (Amsterdam)
Additional Journal Information:
Journal Name: Bioelectrochemistry (Amsterdam); Journal Volume: 129; Journal Issue: C; Journal ID: ISSN 1567-5394
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Hematite; Cytochrome; Electron transfer; Cyclic voltammetry; Adsorption

Citation Formats

Wang, Hanyu, Johs, Alexander, Browning, James F., Tennant, David Alan, and Liang, Liyuan. Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode. United States: N. p., 2019. Web. doi:10.1016/j.bioelechem.2019.05.012.
Wang, Hanyu, Johs, Alexander, Browning, James F., Tennant, David Alan, & Liang, Liyuan. Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode. United States. doi:10.1016/j.bioelechem.2019.05.012.
Wang, Hanyu, Johs, Alexander, Browning, James F., Tennant, David Alan, and Liang, Liyuan. Thu . "Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode". United States. doi:10.1016/j.bioelechem.2019.05.012.
@article{osti_1530101,
title = {Electrochemical properties of the interaction between cytochrome c and a hematite nanowire array electrode},
author = {Wang, Hanyu and Johs, Alexander and Browning, James F. and Tennant, David Alan and Liang, Liyuan},
abstractNote = {We investigate the interaction of horse heart cytochrome c (cyt c) with hematite nanowire array electrodes by cyclic voltammetry to study the electron transfer between redox active proteins and mineral surfaces. Using this model system, we quantify electron transfer rates between cyt c and hematite under varying electric potential and pH conditions. The results are consistent with two cyt c conformations adsorbed at the hematite surface: the native and a partially unfolded form. The partially unfolded protein maintained redox activity, but at a lower redox potential than the native protein. Adsorption of cyt c allowed direct electron transfer between cyt c and hematite, with an interfacial electron transfer rate, k°ET, of 0.4 s-1 for the native form and 0.55 s-1 for the partially unfolded protein at pH 7.07. At pH 4.66, protein adsorption decreased compared to neutral pH and the fraction of partially unfolded protein increased. Additionally, the diffusion controlled electron transfer rate between hematite and the electron shuttling compound anthraquinone-2,6-disulfonate (AQDS) was determined to be k°ET = 8.0·10-3 cm·s-1 at pH 7.07. In conclusion, modulation of electron transfer rates as a result of conformational changes by redox active proteins has broad implications for describing chemical transformations at biological-mineral interfaces.},
doi = {10.1016/j.bioelechem.2019.05.012},
journal = {Bioelectrochemistry (Amsterdam)},
number = C,
volume = 129,
place = {United States},
year = {2019},
month = {5}
}

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This content will become publicly available on May 23, 2020
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